Reference : Crystallographic mapping of β-lactams bound to a D-alanyl-D-alanine peptidase target ...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/91663
Crystallographic mapping of β-lactams bound to a D-alanyl-D-alanine peptidase target enzyme
English
Kelly, Judith A. [University of Connecticut - UCONN > Institute of Material Science > Department of Molecular And Cell Biology > >]
Knox, James R. [University of Connecticut - UCONN > Institute of Material Science > Department of Molecular And Cell Biology > > > >]
Zhao, Haiching C. [University of Connecticut - UCONN > Institute of Material Science > Department of Molecular And Cell Biology > > > >]
Frère, Jean-Marie mailto [Université de Liège - ULiège > > >]
Ghuysen, Jean-Marie [Université de Liège - ULiège > Institut de Chimie > Service de Microbiologie > >]
1989
Journal of Molecular Biology
Academic Press
209
2
281-295
Yes (verified by ORBi)
International
0022-2836
1089-8638
London
United Kingdom
[en] Lactam ; Bacteria ; Actinomycetes ; Actinomycetales ; Streptomycetaceae ; Enzyme ; Antibiotic ; Streptomyces ; Cell wall ; Computer aided analysis ; Electron density map ; X ray diffraction ; Crystallography ; Conserved sequence ; Active site ; Hydrogen bond ; Cephalosporin derivatives ; Penicillin derivatives ; Inhibitor enzyme complex ; Substrate enzyme complex ; Peptidase ; Molecular interaction
[fr] Lactame ; Bactérie ; Actinomycetes ; Actinomycetales ; Streptomycetaceae ; D-Dpeptidase ; Enzyme ; Antibiotique ; Streptomyces ; Paroi cellulaire ; Analyse assistée ; Diagramme densité électronique ; Diffraction RX ; Cristallographie ; Séquence conservée ; Site actif ; Liaison hydrogène ; Céphalosporine dérivé ; Pénicilline dérivé ; Complexe enzyme inhibiteur ; Complexe enzyme substrat ; Peptidase ; Interaction moléculaire
[en] X-ray crystallography has been used to examine the binding of three members of the beta-lactam family of antibiotics to the D-alanyl-D-alanine peptidase from Streptomyces R61, a target of penicillins. Cephalosporin C, the monobactam analog of penicillin G and (2,3)-alpha-methylene benzylpenicillin have been mapped at 2.3 A resolution in the form of acyl-enzyme complexes bound to serine 62. On the basis of the positions of these inhibitors, the binding of a tripeptide substrate for the enzyme, L-lysyl-D-alanyl-D-alanine, has been modeled in the active site. The binding of both inhibitors and substrate is facilitated by hydrogen-bonding interactions with a conserved beta-strand (297-303), which is antiparallel to the beta-lactam's acylamide linkage or the substrate's peptide bond. The active site is similar to that in beta-lactamases.
Researchers ; Professionals
http://hdl.handle.net/2268/91663
10.1016/0022-2836(89)90277-5

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